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1dxh

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{{STRUCTURE_1dxh| PDB=1dxh | SCENE= }}
{{STRUCTURE_1dxh| PDB=1dxh | SCENE= }}
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'''CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA'''
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===CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA===
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==Overview==
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The catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa exhibits allosteric behaviour, with two conformational states of the molecule: an active R form and an inactive T form. The enzyme is a dodecamer with a molecular mass of 455700 Da. Three crystal forms have been obtained. Crystals of allosteric state T are rhombohedral, belonging to the R3 space group, with hexagonal unit-cell parameters a = b = 180.6, c = 122.0 A. They diffract to a resolution of 4.5 A. Two crystal forms for allosteric state R have been obtained, with hexagonal and cubic symmetries. Hexagonal crystals, which diffract to a resolution of 3. 4 A, belong to the space group P6(3) with unit-cell parameters a = b = 140.8, c = 145.6 A. The cubic crystals belong to space group I23, with unit-cell parameter a = 134.32 A and diffract to a resolution better than 2.5 A. In all crystal forms, the dodecamer exhibits a 23 point-group symmetry.
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{{ABSTRACT_PUBMED_10489456}}
==About this Structure==
==About this Structure==
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[[Category: Transcarbamylase]]
[[Category: Transcarbamylase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:23:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:45:56 2008''

Revision as of 20:45, 30 June 2008

Image:1dxh.png

Template:STRUCTURE 1dxh

CATABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA

Template:ABSTRACT PUBMED 10489456

About this Structure

1DXH is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa., Sainz G, Vicat J, Kahn R, Tricot C, Stalon V, Dideberg O, Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1591-3. PMID:10489456

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